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ESF2_DEBHA
ID   ESF2_DEBHA              Reviewed;         303 AA.
AC   Q6BSS5;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Pre-rRNA-processing protein ESF2;
DE   AltName: Full=18S rRNA factor 2;
GN   Name=ESF2; OrderedLocusNames=DEHA2D06600g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Involved in the small subunit (SSU) processome assembly and
CC       function, and in the 18S rRNA synthesis. Required for the early
CC       cleavages at sites A0, A1 and A2 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ESF2/ABP1 family. {ECO:0000305}.
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DR   EMBL; CR382136; CAG86889.2; -; Genomic_DNA.
DR   RefSeq; XP_458745.2; XM_458745.1.
DR   AlphaFoldDB; Q6BSS5; -.
DR   STRING; 4959.XP_458745.2; -.
DR   EnsemblFungi; CAG86889; CAG86889; DEHA2D06600g.
DR   GeneID; 2901551; -.
DR   KEGG; dha:DEHA2D06600g; -.
DR   VEuPathDB; FungiDB:DEHA2D06600g; -.
DR   eggNOG; KOG3152; Eukaryota.
DR   HOGENOM; CLU_054086_0_0_1; -.
DR   InParanoid; Q6BSS5; -.
DR   OMA; TRKHNDF; -.
DR   OrthoDB; 1377351at2759; -.
DR   Proteomes; UP000000599; Chromosome D.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   CDD; cd12263; RRM_ABT1_like; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR039119; ABT1/Esf2.
DR   InterPro; IPR034353; ABT1/ESF2_RRM.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   PANTHER; PTHR12311; PTHR12311; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
PE   3: Inferred from homology;
KW   Nucleus; Reference proteome; Ribosome biogenesis; RNA-binding;
KW   rRNA processing.
FT   CHAIN           1..303
FT                   /note="Pre-rRNA-processing protein ESF2"
FT                   /id="PRO_0000285371"
FT   DOMAIN          96..186
FT                   /note="RRM"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          243..303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        249..295
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   303 AA;  35207 MW;  C8653078A30CC4CE CRC64;
     MIQDESDLDD FEDDEEDDED EKVFNISKKA SHIDNFKNEE SEDEEDLNEE DDDLFMNTDI
     IDEETIENSK QAKNINLKKL TPEQLAKEQK KIKKTGVCYL SKIPPYMKPA KLRSVLSRFG
     KIDRLFLKPE DNSTYTKRVK YGGNKKKNYT AGWVEFINKK DAKLCAGTLN GNKLGGKKSS
     YYYDDIINIK YLSAFKWFDL TQQIAKENEI RQAKLSMELS QQQKLNKSFI NNVEKSKMIN
     NMQNKRKARQ AESGADNSNK EESDIRRNLK QRKLASTRAD AEDELKHKSK PNEKLNDVLS
     KVF
 
 
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